| Structural highlights
2x4u is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | ,
| | Related: | 1uqs, 1bd2, 1hps, 2esv, 2ak4, 1t7k, 1ypz, 1r0a, 1im3, 1hpz, 1uxw, 1i7u, 2vg6, 1qe1, 1npa, 1c16, 1hsa, 1ebk, 1tvr, 1w5y, 1hos, 1gzp, 2axf, 2bnq, 1ikw, 1s6q, 3hvt, 1ec1, 1w72, 2jcc, 2bck, 1de4, 1t05, 2vlk, 1d4i, 1exu, 1meu, 1qrn, 2hla, 1hnv, 1rvr, 1mhe, 1im9, 1eez, 1n6q, 1jht, 1d4h, 1rvn, 1hbv, 1qqd, 1qr1, 1htf, 1rtd, 1zs8, 1hla, 1jgd, 1i1y, 2hmi, 1w5v, 1vgk, 1age, 1ur7, 2bbb, 1hhg, 1s9x, 1a9e, 1duz, 2clr, 3hla, 1m05, 1dlo, 1heg, 1tvb, 1rvl, 2v2w, 1dw6, 2vlr, 1onq, 1yt9, 1a1n, 2bvo, 1htg, 1lp9, 1zsd, 1m6o, 2ban, 1rdh, 1hhk, 1hsb, 1zt4, 1x7q, 1ce6, 1rvo, 1py4, 1syv, 2j8u, 1sys, 1hih, 1hef, 1hni, 1tv6, 1ogt, 1a9m, 1cg9, 1p7q, 1ebz, 2b5j, 1met, 1hys, 1t03, 1q94, 1axa, 1jnj, 1mer, 1npw, 1agb, 3tlh, 2d31, 1suq, 2uxz, 1hvk, 1sbg, 1aqd, 1uwb, 1xz0, 1lds, 1hte, 1tvh, 1hhh, 1hrh, 1xr8, 1hqu, 2bss, 1a1m, 1e28, 2vg7, 2bvp, 1ajv, 1har, 1xr9, 2v2x, 2gj6, 1d4j, 1qlf, 1efx, 2av1, 1tmc, 1hqe, 1qsf, 1ajx, 1duy, 1jge, 1kpr, 1s6p, 1ikv, 1bqm, 2hjl, 1qew, 1ec0, 1w0v, 1k5n, 1rvq, 1ao7, 2bnr, 1xh3, 2be2, 1s9g, 2bst, 1mi5, 1ikx, 1w5w, 1iky, 1qmc, 2h26, 1ec2, 1a1o, 1s9y, 2a83, 1agf, 1oga, 1sv5, 2uy0, 1hmv, 2f8o, 2cii, 1i7r, 1jf1, 1s9e, 2c7u, 1n5y, 2f74, 1e27, 1w0w, 1rvp, 1eet, 1gzq, 1uxs, 1w5x, 2b6a, 1akj, 1hvu, 2hjk, 2vb5, 1ebw, 1r3h, 1agd, 1eey, 1i7t, 1i4f, 1ydp, 1eby, 1j5o, 1hvp, 1mes, 2vll, 1ec3, 2bsr, 2vlj, 1b0r, 1b0g, 1of2, 1hhi, 1qse, 2axg, 1a9b, 1agc, 2bvq, 1hhj, 1qvo, 1s9w, 1ktl, 1bqn, 1a6z, 2vg5, 1rvm, 2cik, 1npv, 2uwe, 1i1f, 2av7, 2x4p, 2x4s, 2x4t, 2x4n, 2x4m, 2x4o, 2x4r, 2x4q |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
High-throughput structure determination of protein-ligand complexes is central in drug development and structural proteomics. To facilitate such high-throughput structure determination we designed an induced replacement strategy. Crystals of a protein complex bound to a photosensitive ligand are exposed to UV light, inducing the departure of the bound ligand, allowing a new ligand to soak in. We exemplify the approach for a class of protein complexes that is especially recalcitrant to high-throughput strategies: the MHC class I proteins. We developed a UV-sensitive, "conditional", peptide ligand whose UV-induced cleavage in the crystals leads to the exchange of the low-affinity lytic fragments for full-length peptides introduced in the crystallant solution. This "in crystallo" exchange is monitored by the loss of seleno-methionine anomalous diffraction signal of the conditional peptide compared to the signal of labeled MHC beta2m subunit. This method has the potential to facilitate high-throughput crystallography in various protein families.
UV-induced ligand exchange in MHC class I protein crystals.,Celie PH, Toebes M, Rodenko B, Ovaa H, Perrakis A, Schumacher TN J Am Chem Soc. 2009 Sep 2;131(34):12298-304. PMID:19655750[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Celie PH, Toebes M, Rodenko B, Ovaa H, Perrakis A, Schumacher TN. UV-induced ligand exchange in MHC class I protein crystals. J Am Chem Soc. 2009 Sep 2;131(34):12298-304. PMID:19655750 doi:10.1021/ja9037559
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